ID V9KX36_CALMI Unreviewed; 419 AA.
AC V9KX36;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Beta-1,4-galactosyltransferase {ECO:0000256|RuleBase:RU368121};
DE Short=Beta-1,4-GalTase {ECO:0000256|RuleBase:RU368121};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU368121};
DE Flags: Fragment;
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFP03666.1};
RN [1] {ECO:0000313|EMBL:AFP03666.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Ovary {ECO:0000313|EMBL:AFP03666.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
CC -!- FUNCTION: Responsible for the synthesis of complex-type N-linked
CC oligosaccharides in many glycoproteins as well as the carbohydrate
CC moieties of glycolipids. {ECO:0000256|ARBA:ARBA00037536,
CC ECO:0000256|RuleBase:RU368121}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-D-glucosamine + UDP-alpha-D-galactose = beta-D-
CC galactosyl-(1->4)-N-acetyl-D-glucosamine + H(+) + UDP;
CC Xref=Rhea:RHEA:17745, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:60152, ChEBI:CHEBI:66914, ChEBI:CHEBI:506227;
CC EC=2.4.1.90; Evidence={ECO:0000256|ARBA:ARBA00036701};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17746;
CC Evidence={ECO:0000256|ARBA:ARBA00036701};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-
CC Cer(d18:1(4E)) + UDP-alpha-D-galactose = a neolactoside
CC nLc4Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:31499,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17006, ChEBI:CHEBI:17103,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.275;
CC Evidence={ECO:0000256|ARBA:ARBA00035795};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31500;
CC Evidence={ECO:0000256|ARBA:ARBA00035795};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside IV(3)-beta-GlcNAc-nLc4Cer + UDP-alpha-D-
CC galactose = beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1')-Cer + H(+)
CC + UDP; Xref=Rhea:RHEA:62548, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914, ChEBI:CHEBI:90357, ChEBI:CHEBI:144378;
CC Evidence={ECO:0000256|ARBA:ARBA00036434};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62549;
CC Evidence={ECO:0000256|ARBA:ARBA00036434};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-
CC galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC derivative + H(+) + UDP; Xref=Rhea:RHEA:22932, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:61631, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:133507; EC=2.4.1.38;
CC Evidence={ECO:0000256|ARBA:ARBA00035817};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22933;
CC Evidence={ECO:0000256|ARBA:ARBA00035817};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucosylceramide + UDP-alpha-D-galactose = a beta-D-
CC galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H(+) + UDP;
CC Xref=Rhea:RHEA:62552, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914, ChEBI:CHEBI:79208, ChEBI:CHEBI:83264;
CC Evidence={ECO:0000256|ARBA:ARBA00043774};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62553;
CC Evidence={ECO:0000256|ARBA:ARBA00043774};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU368121};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU368121}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|RuleBase:RU368121}; Single-pass type II membrane protein
CC {ECO:0000256|RuleBase:RU368121}. Golgi apparatus, Golgi stack membrane
CC {ECO:0000256|ARBA:ARBA00004447}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004447}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family.
CC {ECO:0000256|ARBA:ARBA00005735, ECO:0000256|RuleBase:RU368121}.
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DR EMBL; JW871148; AFP03666.1; -; mRNA.
DR AlphaFoldDB; V9KX36; -.
DR UniPathway; UPA00378; -.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniRule.
DR CDD; cd00899; b4GalT; 1.
DR InterPro; IPR003859; Galactosyl_T.
DR InterPro; IPR027791; Galactosyl_T_C.
DR InterPro; IPR027995; Galactosyl_T_N.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR19300; BETA-1,4-GALACTOSYLTRANSFERASE; 1.
DR PANTHER; PTHR19300:SF33; BETA-1,4-GALACTOSYLTRANSFERASE 3; 1.
DR Pfam; PF02709; Glyco_transf_7C; 1.
DR Pfam; PF13733; Glyco_transf_7N; 1.
DR PRINTS; PR02050; B14GALTRFASE.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW ECO:0000256|RuleBase:RU368121};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU368121};
KW Golgi apparatus {ECO:0000256|RuleBase:RU368121};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Manganese {ECO:0000256|RuleBase:RU368121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368121};
KW Metal-binding {ECO:0000256|RuleBase:RU368121};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968,
KW ECO:0000256|RuleBase:RU368121};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368121};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU368121};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU368121}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368121"
FT DOMAIN 75..208
FT /note="Galactosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13733"
FT DOMAIN 213..289
FT /note="Galactosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02709"
FT REGION 345..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 419
FT /evidence="ECO:0000313|EMBL:AFP03666.1"
SQ SEQUENCE 419 AA; 47748 MW; 359807E17B79C50E CRC64;
MAVCRWLVGR QTLTVLVTAQ LLFVLYVSLS SLHGLPSIFS WTREPVWDYS KTSDVYSNLS
QLPPPANSAS SLPLCPAVSP YLVGPLTISL HLAPSLEIVR YRNPLVGDGG GYSPPDCEAR
SKTALIVPYR NRQTHLRHFL YHIHPFLQRQ QIQYRIYIIH QAGNGTFNRA KLLNVGVKEA
LRDEQWDCLV LHDVDLLPEN DHNLYTCDPH HPKHLSVAMN KFNYRLPYNN YFGGVCALTP
DQYLRMNGFP NEYWGWGGED DDISARVRLT GMTISRPPVS VGHYKMIKHL SDRGNEPNAR
RFDQLFRTGR SWRADGMNSL RFELLTREIT ALYVNVTVDI GDRVRPRARP HTRPHTYVSP
PAHSPSTHMH RQTYSPPPRT APHTHTAPTH TQPTPPHNTQ TPPPHHTHTH THSSATKRE
//
